ID A0A2I1H3I9_9GLOM Unreviewed; 1207 AA.
AC A0A2I1H3I9;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
DE Flags: Fragment;
GN ORFNames=RhiirA4_426021 {ECO:0000313|EMBL:PKY53442.1};
OS Rhizophagus irregularis.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX NCBI_TaxID=588596 {ECO:0000313|EMBL:PKY53442.1, ECO:0000313|Proteomes:UP000234323};
RN [1] {ECO:0000313|EMBL:PKY53442.1, ECO:0000313|Proteomes:UP000234323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A4 {ECO:0000313|EMBL:PKY53442.1,
RC ECO:0000313|Proteomes:UP000234323};
RA Ropars J., Sedzielewska K., Noel J., Charron P., Farinelli L., Marton T.,
RA Kruger M., Pelin A., Brachmann A., Corradi N.;
RT "Genome analyses suggest a sexual origin of heterokaryosis in a supposedly
RT ancient asexual fungus.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.7;
CC Evidence={ECO:0000256|ARBA:ARBA00024632,
CC ECO:0000256|RuleBase:RU000442};
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC {ECO:0000256|ARBA:ARBA00005755, ECO:0000256|RuleBase:RU000442}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PKY53442.1}.
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DR EMBL; LLXI01001387; PKY53442.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I1H3I9; -.
DR VEuPathDB; FungiDB:FUN_021254; -.
DR VEuPathDB; FungiDB:GLOIN_2v1847493; -.
DR VEuPathDB; FungiDB:RhiirA1_403199; -.
DR OrthoDB; 5475218at2759; -.
DR Proteomes; UP000234323; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR Gene3D; 1.10.132.60; DNA polymerase family B, C-terminal domain; 1.
DR Gene3D; 3.30.342.10; DNA Polymerase, chain B, domain 1; 1.
DR Gene3D; 1.10.287.690; Helix hairpin bin; 1.
DR Gene3D; 3.90.1600.10; Palm domain of DNA polymerase; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR InterPro; IPR006172; DNA-dir_DNA_pol_B.
DR InterPro; IPR017964; DNA-dir_DNA_pol_B_CS.
DR InterPro; IPR006133; DNA-dir_DNA_pol_B_exonuc.
DR InterPro; IPR006134; DNA-dir_DNA_pol_B_multi_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR042087; DNA_pol_B_thumb.
DR InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR10322; DNA POLYMERASE CATALYTIC SUBUNIT; 1.
DR PANTHER; PTHR10322:SF23; DNA POLYMERASE DELTA CATALYTIC SUBUNIT; 1.
DR Pfam; PF00136; DNA_pol_B; 2.
DR Pfam; PF03104; DNA_pol_B_exo1; 1.
DR PRINTS; PR00106; DNAPOLB.
DR SMART; SM00486; POLBc; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA replication {ECO:0000256|RuleBase:RU000442};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU000442};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW ECO:0000256|RuleBase:RU000442};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU000442};
KW Reference proteome {ECO:0000313|Proteomes:UP000234323};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442}.
FT DOMAIN 224..461
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 613..756
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 761..1086
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT COILED 735..769
FT /evidence="ECO:0000256|SAM:Coils"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:PKY53442.1"
SQ SEQUENCE 1207 AA; 139192 MW; FBFCA59E14AC5966 CRC64;
EDADLFDSEE IRKPVSQGYT SEEIGKTVNI VNDRGYANEA DEDADLFDSE EIRKPVSQGY
TSEEIGKTVN IVNDRGYANE ADEDADLFDS EEIRKPVSQG YTSEEIGKPG EVIRYSGEEY
LSGIPNRDDL VAENDDPEGS GLSIILNNAL AKQEEIPFMA VDVEESTEFK NGQAWYVLRL
YGPLINGQKV VVTITGIQVF FDIFVPEDLS PDSFKTKIRD ILSGVTKWIK IEHVKAYPFR
GYNPEKKSYL RIYTTNTKQR KIAMKAIQGK KYITASDDQS TYYRKVAREY GIQLSGWSML
REYKYLSGMR VSPLCAHAFW ISIENFHPIE DVATLKDHFP ISALTRDRTL VLTWDIETYS
SRGMGEFPLA EYDEDCVFTI CMTLHWKDDP KPLKQICLVD VESAPDPRWI TIICGSQTNL
LKAFALCWEA FAPDIQLGFN DSQYDWPFVM EKAKSMHLVE WMWKRMSGRQ NRGETSESIL
QWNYYGRLGE TKRVVRQETK YVEDDSDYAS EFRRDAICIK ISPEDAFMSS FLKLPGCVPV
DVRACFKKLY PRSEVEKGSS LKFYLKLCGL DSKADMPFNR LWKFYSNAIE QFCEEEVASI
AYVSLFDTHY RANGMKVRNL LGAYAVKRDM LFSTIPCKEK EKGKYPGAYV FPPKKGIENR
RPVTGLDFAS LYPSLIMAYN FSPEKIILNQ EEADIVGERS RLHKIEFPFN GRTLRAWSVQ
HDNCPKKKGL YPTVLEDLFN KRVALKAKFA LLRKEKERLE KLISSIEGKG KNISNSLKSK
YVSLCFDYNC LNSKQFALKV YMNTFYGEAG NSNSPFFLRE LAGGITTAGQ YNINLVAKYV
TGKGFGIKYG DTDSLYLTCP DRGLSSKEAY WTEMVKITMK VMDDFRNKVN AFLKAKNGTS
YLKMAYEEVL FPVCFTGKKK YFGIAHEEIV NFKPKKPFTK GIDTVKQGQT QIFRFISEKI
MREALDINNE HTIHQIVEDT LKEARHKRWD FNQFIAMAIW KPKVKNQCNQ RFMTRMREKG
LKIPDPGERF SYVLVKGERQ RDEKGRLIAR RIADYMEYPE TVKEYNMEID INHYLEKTLG
MCARFINEDN RYQPPPSHKI MQIRDLDERE KQIDVYSQKE AVKSLKNFIK GEPRVMINTT
SGGFGLRKKS ENPYPKDTLR RIRKKSENPY PKDTLRSIFR PRVIVNTTSV VTQNGPRVMV
NTTSGDF
//
